FBN1_PIG
ID FBN1_PIG Reviewed; 2871 AA.
AC Q9TV36;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Fibrillin-1 {ECO:0000250|UniProtKB:P35555};
DE Contains:
DE RecName: Full=Asprosin {ECO:0000250|UniProtKB:P35555};
DE Flags: Precursor;
GN Name=FBN1 {ECO:0000250|UniProtKB:P35555};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=10036187; DOI=10.1006/geno.1998.5697;
RA Biery N.J., Eldadah Z.A., Moore C.S., Stetten G., Spencer F., Dietz H.C.;
RT "Revised genomic organization of FBN1 and significance for regulated gene
RT expression.";
RL Genomics 56:70-77(1999).
CC -!- FUNCTION: [Fibrillin-1]: Structural component of the 10-12 nm diameter
CC microfibrils of the extracellular matrix, which conveys both structural
CC and regulatory properties to load-bearing connective tissues.
CC Fibrillin-1-containing microfibrils provide long-term force bearing
CC structural support. In tissues such as the lung, blood vessels and
CC skin, microfibrils form the periphery of the elastic fiber, acting as a
CC scaffold for the deposition of elastin. In addition, microfibrils can
CC occur as elastin-independent networks in tissues such as the ciliary
CC zonule, tendon, cornea and glomerulus where they provide tensile
CC strength and have anchoring roles. Fibrillin-1 also plays a key role in
CC tissue homeostasis through specific interactions with growth factors,
CC such as the bone morphogenetic proteins (BMPs), growth and
CC differentiation factors (GDFs) and latent transforming growth factor-
CC beta-binding proteins (LTBPs), cell-surface integrins and other
CC extracellular matrix protein and proteoglycan components. Regulates
CC osteoblast maturation by controlling TGF-beta bioavailability and
CC calibrating TGF-beta and BMP levels, respectively. Negatively regulates
CC osteoclastogenesis by binding and sequestering an osteoclast
CC differentiation and activation factor TNFSF11. This leads to disruption
CC of TNFSF11-induced Ca(2+) signaling and impairment of TNFSF11-mediated
CC nuclear translocation and activation of transcription factor NFATC1
CC which regulates genes important for osteoclast differentiation and
CC function. Mediates cell adhesion via its binding to cell surface
CC receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1. Binds heparin and this
CC interaction plays an important role in the assembly of microfibrils.
CC {ECO:0000250|UniProtKB:P35555, ECO:0000250|UniProtKB:Q61554}.
CC -!- FUNCTION: [Asprosin]: Hormone that targets the liver to increase plasma
CC glucose levels. Secreted by white adipose tissue and circulates in the
CC plasma. Acts in response to fasting and promotes blood glucose
CC elevation by binding to the surface of hepatocytes. Promotes hepatocyte
CC glucose release by activating the protein kinase A activity in the
CC liver, resulting in rapid glucose release into the circulation.
CC {ECO:0000250|UniProtKB:P35555}.
CC -!- SUBUNIT: [Fibrillin-1]: Interacts with COL16A1. Interacts with integrin
CC alpha-V/beta-3. Interacts with ADAMTS10; this interaction promotes
CC microfibril assembly. Interacts with THSD4; this interaction promotes
CC fibril formation. Interacts (via N-terminal domain) with FBLN2 and
CC FBLN5. Interacts with ELN. Forms a ternary complex with ELN and FBLN2
CC or FBLN5 and a significant interaction with ELN seen only in the
CC presence of FBLN2 or FBLN5. Interacts (via N-terminal domain) with
CC LTBP2 (via C-terminal domain) in a Ca(+2)-dependent manner. Interacts
CC (via N-terminal domain) with LTBP1 (via C-terminal domain). Interacts
CC with integrins ITGA5:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6. Interacts (via
CC N-terminal domain) with BMP2, BMP4, BMP7, BMP10 and GDF5. Interacts
CC (via N-terminal domain) with MFAP2 and MFAP5. Interacts with ADAMTSL5.
CC Interacts with MFAP4. Interacts (via N-terminal domain) with TNFSF11 in
CC a Ca(+2)-dependent manner. Interacts (via N-terminal domain) with
CC EFEMP2; this interaction inhibits EFEMP2 binding to LOX and ELN (By
CC similarity). {ECO:0000250|UniProtKB:P35555,
CC ECO:0000250|UniProtKB:Q61554}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P35555}.
CC Note=Fibrillin-1 and Asprosin chains are still linked together during
CC the secretion from cells, but are subsequently separated by furin.
CC {ECO:0000250|UniProtKB:P35555}.
CC -!- SUBCELLULAR LOCATION: [Asprosin]: Secreted
CC {ECO:0000250|UniProtKB:P35555}. Note=Secreted into the plasma.
CC {ECO:0000250|UniProtKB:P35555}.
CC -!- SUBCELLULAR LOCATION: [Fibrillin-1]: Secreted, extracellular space,
CC extracellular matrix {ECO:0000250|UniProtKB:P35555}.
CC -!- PTM: Cleavage of N- and C-terminus by furin is required for
CC incorporation into the extracellular matrix and assembly into
CC microfibrils. The C-terminus, which corresponds to the Asprosin chain,
CC was initially thought to constitute a propeptide. Fibrillin-1 and
CC Asprosin chains are still linked together during the secretion from
CC cells, but are subsequently separated by furin, an essential step for
CC incorporation of Fibrillin-1 into the nascent microfibrils.
CC {ECO:0000250|UniProtKB:P35555}.
CC -!- PTM: [Fibrillin-1]: Forms intermolecular disulfide bonds either with
CC other fibrillin-1 molecules or with other components of the
CC microfibrils. {ECO:0000250|UniProtKB:P35555}.
CC -!- PTM: O-glycosylated on serine residues by POGLUT2 and POGLUT3 which is
CC necessary for efficient protein secretion.
CC {ECO:0000250|UniProtKB:P35555}.
CC -!- SIMILARITY: Belongs to the fibrillin family. {ECO:0000305}.
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DR EMBL; AF073800; AAD50328.1; -; mRNA.
DR RefSeq; NP_001001771.1; NM_001001771.1.
DR BMRB; Q9TV36; -.
DR SMR; Q9TV36; -.
DR STRING; 9823.ENSSSCP00000005017; -.
DR PaxDb; Q9TV36; -.
DR PeptideAtlas; Q9TV36; -.
DR PRIDE; Q9TV36; -.
DR GeneID; 414836; -.
DR KEGG; ssc:414836; -.
DR CTD; 2200; -.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; Q9TV36; -.
DR OrthoDB; 1174178at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0001527; C:microfibril; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0005179; F:hormone activity; ISS:UniProtKB.
DR GO; GO:0034199; P:activation of protein kinase A activity; ISS:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; ISS:UniProtKB.
DR GO; GO:0010737; P:protein kinase A signaling; ISS:UniProtKB.
DR Gene3D; 3.90.290.10; -; 9.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR011398; FBN.
DR InterPro; IPR040872; Fibrillin_U_N.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR017878; TB_dom.
DR InterPro; IPR036773; TB_dom_sf.
DR PANTHER; PTHR24039:SF22; PTHR24039:SF22; 7.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 39.
DR Pfam; PF18193; Fibrillin_U_N; 1.
DR Pfam; PF00683; TB; 9.
DR SMART; SM00181; EGF; 47.
DR SMART; SM00179; EGF_CA; 44.
DR SUPFAM; SSF57184; SSF57184; 10.
DR SUPFAM; SSF57581; SSF57581; 9.
DR PROSITE; PS00010; ASX_HYDROXYL; 41.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 36.
DR PROSITE; PS50026; EGF_3; 43.
DR PROSITE; PS01187; EGF_CA; 41.
DR PROSITE; PS51364; TB; 9.
PE 2: Evidence at transcript level;
KW Calcium; Disulfide bond; EGF-like domain; Extracellular matrix;
KW Glycoprotein; Hormone; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT PROPEP 25..44
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT /id="PRO_0000436885"
FT CHAIN 45..2731
FT /note="Fibrillin-1"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT /id="PRO_0000007583"
FT CHAIN 2732..2871
FT /note="Asprosin"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT /id="PRO_0000436886"
FT DOMAIN 81..112
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 115..146
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 147..178
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 184..236
FT /note="TB 1"
FT DOMAIN 246..287
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 288..329
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 334..389
FT /note="TB 2"
FT DOMAIN 449..489
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 490..529
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 530..571
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 572..612
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 613..653
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 659..711
FT /note="TB 3"
FT DOMAIN 723..764
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 765..806
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 807..846
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 851..902
FT /note="TB 4"
FT DOMAIN 910..951
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 956..1008
FT /note="TB 5"
FT DOMAIN 1028..1069
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1070..1112
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1113..1154
FT /note="EGF-like 17; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1155..1196
FT /note="EGF-like 18; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1197..1237
FT /note="EGF-like 19; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1238..1279
FT /note="EGF-like 20; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1280..1321
FT /note="EGF-like 21; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1322..1362
FT /note="EGF-like 22; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1363..1403
FT /note="EGF-like 23; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1404..1445
FT /note="EGF-like 24; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1446..1486
FT /note="EGF-like 25; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1487..1527
FT /note="EGF-like 26; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1532..1589
FT /note="TB 6"
FT DOMAIN 1606..1647
FT /note="EGF-like 27; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1648..1688
FT /note="EGF-like 28; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1693..1748
FT /note="TB 7"
FT DOMAIN 1766..1807
FT /note="EGF-like 29; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1808..1848
FT /note="EGF-like 30; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1849..1890
FT /note="EGF-like 31; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1891..1929
FT /note="EGF-like 32; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1930..1972
FT /note="EGF-like 33; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1973..2012
FT /note="EGF-like 34; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2013..2054
FT /note="EGF-like 35; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2059..2111
FT /note="TB 8"
FT DOMAIN 2127..2165
FT /note="EGF-like 36; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2166..2205
FT /note="EGF-like 37; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2206..2246
FT /note="EGF-like 38; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2247..2290
FT /note="EGF-like 39; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2291..2332
FT /note="EGF-like 40; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2337..2390
FT /note="TB 9"
FT DOMAIN 2402..2443
FT /note="EGF-like 41; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2444..2484
FT /note="EGF-like 42; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2485..2523
FT /note="EGF-like 43; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2524..2566
FT /note="EGF-like 44; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2567..2606
FT /note="EGF-like 45; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2607..2647
FT /note="EGF-like 46; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2648..2687
FT /note="EGF-like 47; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 29..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..450
FT /note="N-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT REGION 45..81
FT /note="Fibrillin unique N-terminal (FUN) domain"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT REGION 119..329
FT /note="Interaction with MFAP4"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT REGION 195..221
FT /note="Hybrid domain 1"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT REGION 862..887
FT /note="Hybrid domain 2"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT REGION 1528..2731
FT /note="C-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT MOTIF 1541..1543
FT /note="Cell attachment site"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT SITE 44..45
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT SITE 2731..2732
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT MOD_RES 2702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT MOD_RES 2709
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61554"
FT CARBOHYD 268
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 510
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1135
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1218
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1302
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1345
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1386
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1508
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1628
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1830
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1871
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1902
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1911
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1953
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2035
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2077
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2148
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2227
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2313
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2465
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2547
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2628
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2750
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..68
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT DISULFID 67..80
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT DISULFID 85..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 89..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 102..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 119..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 123..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 136..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 150..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 154..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 168..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 250..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 257..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 273..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 292..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 299..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 315..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 453..465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 460..474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 476..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 494..504
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 499..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 515..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 534..546
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 541..555
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 557..570
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 576..587
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 582..596
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 598..611
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 617..628
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 623..637
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 639..652
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 727..739
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 734..748
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 750..763
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 769..781
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 776..790
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 792..805
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 811..821
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 816..830
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 832..845
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 853..875
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 862..887
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 876..890
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 896..908
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 914..926
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 921..935
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 937..950
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1032..1044
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1039..1053
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1055..1068
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1074..1086
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1081..1095
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1097..1111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1117..1129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1124..1138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1140..1153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1159..1171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1201..1212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1208..1221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1223..1236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1242..1254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1249..1263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1265..1278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1284..1296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1291..1305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1307..1320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1326..1339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1333..1348
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1350..1361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1367..1380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1374..1389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1391..1402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1408..1420
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1415..1429
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1450..1461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1456..1470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1472..1485
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1491..1502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1497..1511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1513..1526
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1534..1562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1549..1574
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1563..1577
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1564..1589
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1610..1622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1617..1631
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1633..1646
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1652..1663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1658..1672
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1674..1687
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1770..1782
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1777..1791
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1793..1806
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1812..1824
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1818..1833
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1835..1847
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1853..1865
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1860..1874
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1876..1889
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1895..1905
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1900..1914
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1916..1928
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1934..1947
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1942..1956
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1958..1971
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1977..1989
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1984..1998
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2000..2011
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2017..2029
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2024..2038
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2040..2053
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2061..2083
FT /evidence="ECO:0000250|UniProtKB:P35555,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2070..2096
FT /evidence="ECO:0000250|UniProtKB:P35555,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2084..2099
FT /evidence="ECO:0000250|UniProtKB:P35555,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2085..2111
FT /evidence="ECO:0000250|UniProtKB:P35555,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2131..2142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2137..2151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2153..2164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2170..2181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2176..2190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2192..2204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2210..2221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2217..2230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2232..2245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2251..2265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2258..2274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2276..2289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2295..2307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2302..2316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2318..2331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2406..2418
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2413..2427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2429..2442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2448..2459
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2455..2468
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2470..2483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2489..2500
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2496..2509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2511..2522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2528..2541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2535..2550
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2552..2565
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2571..2581
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2577..2590
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2592..2605
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2611..2622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2617..2631
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2633..2646
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2652..2663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2659..2672
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2674..2686
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2871 AA; 312699 MW; 7A0E40FA8CA65F07 CRC64;
MRRGRLLEVA LGFTVLLASY TSHRAEANLE AGNGKETRAS RAKRRGGGGH DALKGPNVCG
SRYNAYCCPG WKTLPGGNQC IVPICRHSCG DGFCSRPNMC TCPSGQIAPS CGSRSIQHCN
IRCMNGGSCS DDHCLCQKGY IGTHCGQPVC ESGCLNGGRC VAPNRCACTY GFTGPQCERD
YRTGPCFTVV SNQMCQGQLS GIVCTKTLCC ATVGRAWGHP CEMCPAQPHP CRRGFIPNIR
TGACQDVDEC QAIPGLCQGG NCINTVGSFE CKCPAGHKFN EVSQKCEDID ECSTIPGICD
GGECTNTVSS YFCKCPPGFY TSPDGTRCID VRPGYCYTAL TNGRCSNQLP QSITKMQCCC
DVGRCWSPGV TVTPEMCPIR ATEDFNKLCS VPMVVPERPG YPSPPLGPIP PVHPVPPGFP
PGPQIPVPRP PVEYPYPSRE PPRVLPVNVT DYCQLFRYLC HNGRCIPTPG SYRCECNKGF
QLDLRGECID VDECEKNPCA GGECINNQGS YTCQCRPGYQ STLTRTECRD IDECLQNGRI
CNNGRCINTD GSFHCVCNAG FHVTRDGKNC EDMDECSIRN MCLNGMCINE DGSFKCICKP
GFQLASDGRY CKDINECETS GICMNGRCVN TDGSYRCECF PGLAVGLDGR VCVDTHMRST
CYGGYKRGQC VKPLFGAVTK SECCCASTEY AFGEPCQPCP SQNSAEYQAL CSSGPGMTSA
GSDINECALD PDICPNGICE NLRGTYKCIC NSGYEVDSTG KNCVDINECV LNSLLCDNGQ
CRNTPGSFVC TCPKGFIYKP DLKTCEDIDE CESSPCINGV CKNSPGSFIC ECSSESTLDP
TKTICIETIK GTCWQTIIDG RCEININGAT LKSQCCSSLG AAWGSPCTPC QVDPICGKGY
SRIKGTQCED IDECEVFPGV CKNGLCVNSK GSFKCQCPNG MTLDATGRIC LDIRLETCFL
RYEDEECTLP VVGRHRMDAC CCSVGAAWGT EECEECPPRN TPEYEELCPR GPGFATKEIT
NGKPFFKDIN ECKMIPNLCT HGKCRNTIGS FKCRCDSGFA LDSEERNCID IDECRISPDL
CGRGQCVNTP GDFECKCDEG YESGFMMMKN CMDIDECQRD PLLCRGGVCL NTEGSYRCEC
PSGHQMSPNI SACIDINECE LSAHLCPHGR CVNLIGKYQR ARNPGYHSTP DRLFCVDIDE
CSIMNGGCET FCTNSEGSYE CSCQPGFALM PDQRSCTDID ECEDNPNICD GGQCTNIPGE
YRCLCYDGFM ASEDMKTCVD VNECDLNPNI CLSGTCENTK GSFICHCDMG YSGKKGKTGC
TDINECEIGA HNCDRHAVCT NTAGSFNCSC SPGWIGDGIK CTDLDECSNG THMCSQHADC
KNTMGSYRCL CKEGYTGDGF TCADLDECSE NVKLCGNVQC LYAPGGYHCE YDMGFVPSAD
RKSCVDSDEC SLPNICVFGT CHNLPGLFRC ECEIGYELDR SGGNCTDVNE CLEPPTCISG
NCVNTPGSYT CVCPPDFELN PTRVGCVDTR SGNCYLDVRP RGDNGDTACS NEIGVGVSKA
SCCCSLGKAW GTPCEQCPPV NTSEYKILCP GGEGFRPNPI TVILEDIDEC QELPGLCQGG
KCINTFGSFQ CRCPTGYYLN EDTRVCDDVN ECETPGICGP GTCYNTVGNY TCICPPDYMQ
VNGGNNCMDM RRSLCYRNYY ADNQTCDGEL LFNMTKKMCC CSYNIGRAWN KPCEQCPIPS
TDEFATLCGS QRPGFVIDIY TGLPVDIDEC REIPGVCENG VCINMVGSFR CECPVGFFYN
DKLLVCEDID ECQNGPVCQR NAECINTAGS YRCDCKPGYR FTSTGQCNDR NECQEIPNIC
SHGQCIDTVG SFYCLCHTGF KTNADQTMCL DINECERDAC GNGTCRNTIG SFNCRCNHGF
ILSHNNDCID VDECATGNGN LCRNGQCINT VGSFQCQCNE GYEVAPDGRT CVDINECLLE
PGKCAPGTCQ NLDGSYRCIC PPGYSLQNDK CEDIDECVEE PEICALGTCS NTEGSFKCLC
PDGFSLSSTG RRCQDLRMSY CYAKFEGGKC SSPKSRNHSK QECCCALKGE GWGDPCELCP
TEPDEAFRQI CPYGSGIIVG PDDSAVDMDE CKEPDVCKHG QCINTDGSYR CECPFGYILE
GNECVDTDEC SVGNPCGNGT CKNVIGGFEC TCEEGFEPGP MMTCEDINEC AQNPLLCAFR
CVNTYGSYEC KCPTGYVLRE DRRMCKDEDE CEEGKHDCAE KQMECKNLIG MYICICGPGY
QRRPDGEGCV DENECQTKPG ICENGRCLNT RGSYTCECND GFTASPTQDE CLDNREGYCF
TEVLQNMCQI GSSNRNPVTK SECCCDGGRG WGPHCEICPF QGTVAFKKLC PHGRGFMTNG
ADIDECKVIH DVCRNGECIN DRGSYHCICK TGYTPDITGT ACVDLNECNQ APKPCNFICK
NTEGSYQCSC PKGYILQEDG RSCKDLDECA TKQHNCQFLC VNTIGSFACK CPPGFTQHHT
ACIDNNECTS DINLCGAKGI CQNTPGSFTC ECQRGFSLDQ SGASCEDVDE CEGNHRCQHG
CQNIIGGYRC SCPQGYLQHY QWNQCVDENE CLSAHICGGA SCHNTLGSYK CMCPAGFQYE
QFSGGCQDIN ECGSSQAPCS YGCSNTEGGY LCGCPPGYFR IGQGHCVSGM GMGRGSPEPP
ASGEMDDNSL SPEACYECKI NGYPKRGRKR RSTNETDAFN IEDQPETESN VSLASWDVEK
TAVFAFNISH ISNKVRILEL LPALTTLTNH NRYLIESGNE NGFFKINQKE GISYLHFTKK
KPVAGTYSLQ ISSTPLYKKK ELNQLEDKYD KDYLSGELGD NLKMKIQILL H
